1zpq: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='1zpq' size='340' side='right'caption='[[1zpq]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1zpq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZPQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1zpq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZPQ FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CII ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10710 Bacteriophage lambda])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zpq OCA], [https://pdbe.org/1zpq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zpq RCSB], [https://www.ebi.ac.uk/pdbsum/1zpq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zpq ProSAT], [https://www.topsan.org/Proteins/MCSG/1zpq TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/RPC2_LAMBD RPC2_LAMBD]] This protein and protein CIII form a complex that is involved in the initiation of lysogeny. The complex binds at either of the cy regulatory sites preceding the CI repressor protein and integrase coding regions and induces transcription of these genes.
+[https://www.uniprot.org/uniprot/RPC2_LAMBD RPC2_LAMBD] This protein and protein CIII form a complex that is involved in the initiation of lysogeny. The complex binds at either of the cy regulatory sites preceding the CI repressor protein and integrase coding regions and induces transcription of these genes.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 19: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zpq ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The tetrameric cII protein from bacteriophage lambda activates transcription from the phage promoters P(RE), P(I), and P(AQ) by binding to two direct repeats that flank the promoter -35 element. Here, we present the X-ray crystal structure of cII alone (2.8 A resolution) and in complex with its DNA operator from P(RE) (1.7 A resolution). The structures provide a basis for modeling of the activation complex with the RNA polymerase holoenzyme, and point to the key role for the RNA polymerase alpha subunit C-terminal domain (alphaCTD) in cII-dependent activation, which forms a bridge of protein/protein interactions between cII and the RNA polymerase sigma subunit. The model makes specific predictions for protein/protein interactions between cII and alphaCTD, and between alphaCTD and sigma, which are supported by previous genetic studies.
-Crystal structure of bacteriophage lambda cII and its DNA complex.,Jain D, Kim Y, Maxwell KL, Beasley S, Zhang R, Gussin GN, Edwards AM, Darst SA Mol Cell. 2005 Jul 22;19(2):259-69. PMID:16039594<ref>PMID:16039594</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1zpq" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacteriophage lambda]]
+[[Category: Escherichia virus Lambda]]
 [[Category: Large Structures]]
-[[Category: Beasley, S]]
+[[Category: Beasley S]]
-[[Category: Darst, S A]]
+[[Category: Darst SA]]
-[[Category: Edwards, A M]]
+[[Category: Edwards AM]]
-[[Category: Gussin, G N]]
+[[Category: Gussin GN]]
-[[Category: Jain, D]]
+[[Category: Jain D]]
-[[Category: Joachimiak, A]]
+[[Category: Joachimiak A]]
-[[Category: Kim, Y]]
+[[Category: Kim Y]]
-[[Category: Structural genomic]]
+[[Category: Maxwell KL]]
-[[Category: Maxwell, K L]]
-[[Category: Helix-turn-helix]]
-[[Category: Mcsg]]
-[[Category: PSI, Protein structure initiative]]
-[[Category: Transcription activation]]
-[[Category: Transcription activator]]